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Protein

ATP synthase subunit c, chloroplastic

Gene

atpH

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F1 containing the extramembraneous catalytic core and F0 containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 14 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits.

Miscellaneous

In plastids the F-type ATPase is also known as CF1CF0.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei61Reversibly protonated during proton transportUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport
LigandLipid-binding

Enzyme and pathway databases

BRENDAi3.6.3.14 5812

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit c, chloroplasticUniRule annotation
Alternative name(s):
ATP synthase F(0) sector subunit cUniRule annotation
ATPase subunit IIIUniRule annotation
F-type ATPase subunit cUniRule annotation
Short name:
F-ATPase subunit cUniRule annotation
Lipid-binding proteinUniRule annotation
Gene namesi
Name:atpHUniRule annotation
Encoded oniPlastid; Chloroplast
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia
Proteomesi
  • UP000054095 Componenti: Chloroplast

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei3 – 23HelicalUniRule annotationAdd BLAST21
Transmembranei57 – 77HelicalUniRule annotationAdd BLAST21

Keywords - Cellular componenti

CF(0), Chloroplast, Membrane, Plastid, Thylakoid

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2366567

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001122051 – 81ATP synthase subunit c, chloroplasticAdd BLAST81

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-formylmethionine1 Publication1

Keywords - PTMi

Formylation

Interactioni

Subunit structurei

F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane proton channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has four main subunits: a1, b1, b'1 and c(14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F1 is attached to F0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains.1 Publication

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2W5JX-ray3.80A/B/C/D/E/F/G/H/I/J/K/L/M/V2-79[»]
ProteinModelPortaliP69447
SMRiP69447
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69447

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK02110

Family and domain databases

Gene3Di1.20.20.10, 1 hit
HAMAPiMF_01396 ATP_synth_c_bact, 1 hit
InterProiView protein in InterPro
IPR005953 ATP_synth_csu_bac/chlpt
IPR000454 ATP_synth_F0_csu
IPR020537 ATP_synth_F0_csu_DDCD_BS
IPR038662 ATP_synth_F0_csu_sf
IPR002379 ATPase_proteolipid_c-like_dom
IPR035921 F/V-ATP_Csub_sf
PANTHERiPTHR10031 PTHR10031, 1 hit
PfamiView protein in Pfam
PF00137 ATP-synt_C, 1 hit
PRINTSiPR00124 ATPASEC
SUPFAMiSSF81333 SSF81333, 1 hit
TIGRFAMsiTIGR01260 ATP_synt_c, 1 hit
PROSITEiView protein in PROSITE
PS00605 ATPASE_C, 1 hit

Sequencei

Sequence statusi: Complete.

P69447-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPLIAAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR
60 70 80
GTLLLSLAFM EALTIYGLVV ALALLFANPF V
Length:81
Mass (Da):7,974
Last modified:July 21, 1986 - v1
Checksum:i75F8DBD4F23A896D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03775 Genomic DNA Translation: CAA27402.1
AJ400848 Genomic DNA Translation: CAB88712.1
PIRiS14423 LWSPA
RefSeqiNP_054919.1, NC_002202.1

Genome annotation databases

GeneIDi2715579
KEGGisoe:2715579

Similar proteinsi

Entry informationi

Entry nameiATPH_SPIOL
AccessioniPrimary (citable) accession number: P69447
Secondary accession number(s): P00843, Q33180, Q9XPT1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 25, 2018
This is version 73 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health